Hyperglycosylation of hen egg white lysozyme in yeast

Nakamura, Soichiro; Takasaki, H; Kobayashi, Kunihiko; Kato, Akio

doi:10.1016/s0021-9258(18)31445-5

Cited by 70 publications

(31 citation statements)

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“…However, the general use of lysozyme in winemaking is limited because of its low cost-ef®ciency. This has encouraged efforts to develop lysozyme-producing S. cerevisiae strains [106]. The lysozyme-encoding gene from chicken egg white was successfully expressed in E. coli and S. cerevisiae.…”

Section: Wine Yeasts Producing Antimicrobial Enzymesmentioning

confidence: 99%

Tailoring wine yeast for the new millennium: novel approaches to the ancient art of winemaking

Pretorius

2000

Yeast

962

406

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Yeasts are predominant in the ancient and complex process of winemaking. In spontaneous fermentations, there is a progressive growth pattern of indigenous yeasts, with the ®nal stages invariably being dominated by the alcohol-tolerant strains of Saccharomyces cerevisiae. This species is universally known as the `wine yeast' and is widely preferred for initiating wine fermentations. The primary role of wine yeast is to catalyze the rapid, complete and ef®cient conversion of grape sugars to ethanol, carbon dioxide and other minor, but important, metabolites without the development of off-¯avours. However, due to the demanding nature of modern winemaking practices and sophisticated wine markets, there is an ever-growing quest for specialized wine yeast strains possessing a wide range of optimized, improved or novel oenological properties. This review highlights the wealth of untapped indigenous yeasts with oenological potential, the complexity of wine yeasts' genetic features and the genetic techniques often used in strain development. The current status of genetically improved wine yeasts and potential targets for further strain development are outlined. In light of the limited knowledge of industrial wine yeasts' complex genomes and the daunting challenges to comply with strict statutory regulations and consumer demands regarding the future use of genetically modi®ed strains, this review cautions against unrealistic expectations over the short term. However, the staggering potential advantages of improved wine yeasts to both the winemaker and consumer in the third millennium are pointed out.

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Section: Wine Yeasts Producing Antimicrobial Enzymesmentioning

confidence: 99%

Tailoring wine yeast for the new millennium: novel approaches to the ancient art of winemaking

Pretorius

2000

Yeast

962

406

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“…S. cerevisiae has long been an efficient cell factory for the expression of eukaryotic proteins and can perform complex post-translational modifications, such as glycosylation, disulfide formation, phosphorylation, and acylation. For glycoproteins, however, S. cerevisiae typically produces high-mannose type glycan stretches, which can be antigenic for recombinant mammalian proteins . Nonetheless, the glycosylation pathway in yeast is similar to that of the insect, by which glycoproteins are modified with heterogeneous mannose-type N-glycan structures .…”

Section: Discussionmentioning

confidence: 99%

“…For glycoproteins, however, S. cerevisiae typically produces high-mannose type glycan stretches, which can be antigenic for recombinant mammalian proteins. 58 Nonetheless, the glycosylation pathway in yeast is similar to that of the insect, by which glycoproteins are modified with heterogeneous mannose-type N-glycan structures. 59 In particular, the yeast and insect systems have identical steps of glycosylation in the endoplasmic reticulum (ER), which are proved to be intimately coupled with the quality control of protein folding.…”

Section: ■ Discussionmentioning

confidence: 99%

Yeast Surface Display of Antheraea pernyi Lysozyme Revealed α-Helical Antibacterial Peptides in Its N-Terminal Domain

Wen

Mao

Yao

et al. 2018

J. Agric. Food Chem.

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The present study investigated a novel lysozyme ApLyz from the Chinese oak silkmoth, Antheraea pernyi, for its active expression with N- or C-terminus fused to the yeast cell surface, and the antimicrobial activities of the corresponding expressed lysozymes were evaluated. The bactericidal activity of C-terminal fusion of ApLyz surpassed that of the N-terminal fusion, which revealed the implication of an N-terminal stretch of ApLyz in the bactericidal function based on the structural mobility of this region. Two N-terminal peptides of ApLyz (residues 1-15 and 1-32), which primarily consist of amphiphilic α-helices, exerted similar bactericidal efficacy and had a strong preference for the Gram-negative strains. Further investigation revealed that the N-terminal peptides are membrane-targeting peptides causing cell permeabilization and also possess nonmembrane disturbing bactericidal mechanism. Overall, in addition to the key findings of novel bactericidal peptides from silkmoth lysozyme, this work laid the foundation for future improvement of ApLyz by protein engineering.

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“…For MPs such as the hA 2A receptor, S. cerevisiae , or Baker's yeast remains one of the best platforms to express and purify the receptor in a form suitable for structural characterization (O'Malley et al, 2009). Another important consideration when expressing MPs in S. cerevisiae is the propensity for hyper‐glycosylation with mannose sugar residues, which was previously reported for lysozyme (Butz et al, 2003; Nakamura et al, 1993; Young & Robinson, 2014). Subsequent studies have been carried out in an attempt to predict sites of glycosylation as well (Conde et al, 2004).…”

Section: Introductionmentioning

confidence: 96%

Predicted N‐terminal N‐linked glycosylation sites may underlie membrane protein expression patterns in Saccharomyces cerevisiae

Karki

Rimal

Rieth

2021

Yeast

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N‐linked glycosylation is one type of posttranslational modification that proteins undergo during expression. The following describes the effects of N‐linked glycosylation on high‐level membrane protein expression in yeast with an emphasis on Saccharomyces cerevisiae. N‐linked glycosylation is highlighted here as an important consideration when preparing membrane protein gene constructs for expression in S. cerevisiae, which continues to be used as a workhorse in both research and industrial applications. Non‐native N‐linked glycosylation commonly occurs during the heterologous expression of mammalian proteins in many yeast species which can have important immunological consequences when used in the production of biotherapeutic proteins or peptides. Further, non‐native N‐linked glycosylation can lead to improper protein folding and premature degradation, which can impede high‐level expression yields and hinder downstream analysis. Multiple strategies are presented in this article, which suggest different methods that can be implemented to circumvent the unwanted consequences of N‐linked glycosylation during the expression process. These considerations may have long‐term benefits for high‐level protein production in S. cerevisiae across a broad spectrum of expression targets with special emphasis placed on G‐protein coupled receptors, one of the largest families of membrane proteins.

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Hyperglycosylation of hen egg white lysozyme in yeast

Cited by 70 publications

References 0 publications

Tailoring wine yeast for the new millennium: novel approaches to the ancient art of winemaking

Tailoring wine yeast for the new millennium: novel approaches to the ancient art of winemaking

Yeast Surface Display of Antheraea pernyi Lysozyme Revealed α-Helical Antibacterial Peptides in Its N-Terminal Domain

Predicted N‐terminal N‐linked glycosylation sites may underlie membrane protein expression patterns in Saccharomyces cerevisiae

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